CD47 signaling pathways controlling cellular differentiation and responses to stress

References

• Adams JC, Bentley AA, Kvansakul M, et al. (2008). Extracellular matrix retention of thrombospondin 1 is controlled by its conserved C-terminal region. J Cell Sci 121:784–95
   PubMed Web of Science ®Google Scholar
• Avent ND, Madgett TE, Lee ZE, et al. (2006). Molecular biology of Rh proteins and relevance to molecular medicine. Expert Rev Mol Med 8:1–20
   PubMedGoogle Scholar
• Azcutia V, Routledge M, Williams MR, et al. (2013). CD47 plays a critical role in T-cell recruitment by regulation of LFA-1 and VLA-4 integrin adhesive functions. Mol Biol Cell 24:3358–68
   PubMed Web of Science ®Google Scholar
• Bamberger ME, Harris ME, Mcdonald DR, et al. (2003). A cell surface receptor complex for fibrillar beta-amyloid mediates microglial activation. J Neurosci 23:2665–74
   PubMed Web of Science ®Google Scholar
• Barazi HO, Li Z, Cashel JA, et al. (2002). Regulation of integrin function by CD47 ligands. Differential effects on avb3 and a4b1 integrin-mediated adhesion. J Biol Chem 277:42859–66
   Google Scholar
• Barclay AN, Van Den Berg TK. (2014). The interaction between signal regulatory protein alpha (SIRPalpha) and CD47: structure, function, and therapeutic target. Annu Rev Immunol 32:25–50
   PubMed Web of Science ®Google Scholar
• Bauer EM, Qin Y, Miller TW, et al. (2010). Thrombospondin-1 supports blood pressure by limiting eNOS activation and endothelial-dependent vasorelaxation. Cardiovasc Res 88:471–81
   PubMed Web of Science ®Google Scholar
• Bernardi B, Guidetti GF, Campus F, et al. (2006). The small GTPase Rap1b regulates the cross talk between platelet integrin alpha2beta1 and integrin alphaIIbbeta3. Blood 107:2728–35
   PubMed Web of Science ®Google Scholar
• Bjorkoy G, Lamark T, Pankiv S, et al. (2009). Monitoring autophagic degradation of p62/SQSTM1. Methods Enzymol 452:181–97
   PubMed Web of Science ®Google Scholar
• Bras M, Yuste VJ, Roue G, et al. (2007). Drp1 mediates caspase-independent type III cell death in normal and leukemic cells. Mol Cell Biol 27:7073–88
   PubMed Web of Science ®Google Scholar
• Brittain JE, Han J, Ataga KI, et al. (2004). Mechanism of CD47-induced alpha4beta1 integrin activation and adhesion in sickle reticulocytes. J Biol Chem 279:42393–402
   PubMed Web of Science ®Google Scholar
• Brooke G, Holbrook JD, Brown MH, Barclay AN. (2004). Human lymphocytes interact directly with CD47 through a novel member of the signal regulatory protein (SIRP) family. J Immunol 173:2562–70
   PubMed Web of Science ®Google Scholar
• Burger P, De Korte D, Van Den Berg TK, Van Bruggen R. (2012). CD47 in erythrocyte ageing and clearance – the Dutch point of view. Transfus Med Hemother 39:348–52
   PubMed Web of Science ®Google Scholar
• Cambot M, Mazurier C, Canoui-Poitrine F, et al. (2013). In vitro generated Rh(null) red cells recapitulate the in vivo deficiency: a model for rare blood group phenotypes and erythroid membrane disorders. Am J Hematol 88:343–9
   PubMed Web of Science ®Google Scholar
• Campbell IG, Freemont PS, Foulkes W, Trowsdale J. (1992). An ovarian tumor marker with homology to vaccinia virus contains an IgV-like region and multiple transmembrane domains. Cancer Res 52:5416–20
   PubMed Web of Science ®Google Scholar
• Cant CA, Ullrich A. (2001). Signal regulation by family conspiracy. Cell Mol Life Sci 58:117–24
   PubMed Web of Science ®Google Scholar
• Chandrasekaran S, Guo N, Rodrigues RG, et al. (1999). Pro-adhesive and chemotactic activities of thrombospondin-1 for breast carcinoma cella are mediated by a3b1 integrin and regulated by insulin-like growth factor-1 and CD98. J Biol Chem 274:11408–16
   PubMed Web of Science ®Google Scholar
• Chang CR, Blackstone C. (2007). Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology. J Biol Chem 282:21583–7
   PubMed Web of Science ®Google Scholar
• Chao MP, Alizadeh AA, Tang C, et al. (2011). Therapeutic antibody targeting of CD47 eliminates human acute lymphoblastic leukemia. Cancer Res 71:1374–84
   PubMed Web of Science ®Google Scholar
• Chao MP, Weissman IL, Majeti R. (2012). The CD47-SIRPalpha pathway in cancer immune evasion and potential therapeutic implications. Curr Opin Immunol 24:225–32
   PubMed Web of Science ®Google Scholar
• Chu LY, Ramakrishnan DP, Silverstein RL. (2013). Thrombospondin-1 modulates VEGF signaling via CD36 by recruiting SHP-1 to VEGFR2 complex in microvascular endothelial cells. Blood 122:1822–32
   PubMed Web of Science ®Google Scholar
• Chung J, Gao AG, Frazier WA. (1997). Thrombspondin acts via integrin-associated protein to activate the platelet integrin aIIbb3. J Biol Chem 272:14740–6
   PubMed Web of Science ®Google Scholar
• Chung J, Wang XQ, Lindberg FP, Frazier WA. (1999). Thrombospondin-1 acts via IAP/CD47 to synergize with collagen in alpha2beta1-mediated platelet activation. Blood 94:642–8
   PubMed Web of Science ®Google Scholar
• Csanyi G, Yao M, Rodriguez AI, et al. (2012). Thrombospondin-1 regulates blood flow via CD47 receptor-mediated activation of NADPH oxidase 1. Arterioscler Thromb Vasc Biol 32:2966–73
   PubMed Web of Science ®Google Scholar
• Dahl KN, Westhoff CM, Discher DE. (2003). Fractional attachment of CD47 (IAP) to the erythrocyte cytoskeleton and visual colocalization with Rh protein complexes. Blood 101:1194–9
   PubMed Web of Science ®Google Scholar
• Dang CV. (2013). MYC, metabolism, cell growth, and tumorigenesis. Cold Spring Harb Perspect Med 3. doi: 10.1101/cshperspect.a014217
   Google Scholar
• Dong X, Mi LZ, Zhu J, et al. (2012). alpha(V)beta(3) integrin crystal structures and their functional implications. Biochemistry 51:8814–28
   PubMed Web of Science ®Google Scholar
• Dorahy DJ, Thorne RF, Fecondo JV, Burns GF. (1997). Stimulation of platelet activation and aggregation by a carboxyl-terminal peptide from thrombospondin binding to the integrin-associated protein receptor. J Biol Chem 272:1323–30
   PubMed Web of Science ®Google Scholar
• Drbal K, Cerny J, Angelisova P, et al. (2000). CDw149 antibodies recognize a clustered subset of CD47 molecules associated with cytoplasmic signaling molecules. Tissue Antigens 56:258–67
   PubMed Web of Science ®Google Scholar
• Edris B, Weiskopf K, Volkmer AK, et al. (2012). Antibody therapy targeting the CD47 protein is effective in a model of aggressive metastatic leiomyosarcoma. Proc Natl Acad Sci USA 109:6656–61
   PubMed Web of Science ®Google Scholar
• Flatt JF, Musa RH, Ayob Y, et al. (2012). Study of the D-phenotype reveals erythrocyte membrane alterations in the absence of RHCE. Br J Haematol 158:262–73
   PubMed Web of Science ®Google Scholar
• Floquet N, Dedieu S, Martiny L, et al. (2008). Human thrombospondin's (TSP-1) C-terminal domain opens to interact with the CD-47 receptor: a molecular modeling study. Arch Biochem Biophys 478:103–9
   PubMed Web of Science ®Google Scholar
• Frazier EP, Isenberg JS, Shiva S, et al. (2011). Age-dependent regulation of skeletal muscle mitochondria by the thrombospondin-1 receptor CD47. Matrix Biol 30:154–61
   PubMed Web of Science ®Google Scholar
• Frazier WA, Gao A-G, Dimitry J, et al. (1999). The thrombospondin receptor integrin-associated protein (CD47) functionally couples to heterotrimeric Gi. J Biol Chem 274:8554–60
   PubMed Web of Science ®Google Scholar
• Fujimoto TT, Katsutani S, Shimomura T, Fujimura K. (2003). Thrombospondin-bound integrin-associated protein (CD47) physically and functionally modifies integrin alphaIIbbeta3 by its extracellular domain. J Biol Chem 278:26655–65
   PubMed Web of Science ®Google Scholar
• Gao A-G, Lindberg FP, Finn MB, et al. (1996). Integrin-associated protein is a receptor for the C-terminal domain of thrombospondin. J Biol Chem 271:21–4
   PubMed Web of Science ®Google Scholar
• Grimbert P, Bouguermouh S, Baba N, et al. (2006). Thrombospondin/CD47 interaction: a pathway to generate regulatory T cells from human CD4 + CD25− T cells in response to inflammation. J Immunol 177:3534–41
   PubMed Web of Science ®Google Scholar
• Grunewald FS, Prota AE, Giese A, Ballmer-Hofer K. (2010). Structure–function analysis of VEGF receptor activation and the role of coreceptors in angiogenic signaling. Biochim Biophys Acta 1804:567–80
   PubMed Web of Science ®Google Scholar
• Guo N, Zabrenetzky VS, Chandrasekaran L, et al. (1998). Differential Roles of protein kinase C and pertussis toxin-sensitive G-binding proteins in modulation of melanoma cell proliferation and motility by thrombospondin-1. Cancer Res 58:3154–62
   PubMed Web of Science ®Google Scholar
• Gupta K, Gupta P, Wild R, et al. (1999). Binding and displacement of vascular endothelial growth factor (VEGF) by thrombospondin: effect on human microvascular endothelial cell proliferation and angiogenesis. Angiogenesis 3:147–58
   PubMedGoogle Scholar
• Hanna RA, Quinsay MN, Orogo AM, et al. (2012). Microtubule-associated protein 1 light chain 3 (LC3) interacts with Bnip3 protein to selectively remove endoplasmic reticulum and mitochondria via autophagy. J Biol Chem 287:19094–104
   PubMed Web of Science ®Google Scholar
• Hatherley D, Graham SC, Turner J, et al. (2008). Paired receptor specificity explained by structures of signal regulatory proteins alone and complexed with CD47. Mol Cell 31:266–77
   PubMed Web of Science ®Google Scholar
• Isenberg JS, Annis DS, Pendrak ML, et al. (2009a). Differential interactions of thrombospondin-1, -2, and -4 with CD47 and effects on cGMP signaling and ischemic injury responses. J Biol Chem 284:1116–25
   PubMed Web of Science ®Google Scholar
• Isenberg JS, Hyodo F, Pappan LK, et al. (2007a). Blocking thrombospondin-1/CD47 signaling alleviates deleterious effects of aging on tissue responses to ischemia. Arterioscler Thromb Vasc Biol 27:2582–8
   PubMed Web of Science ®Google Scholar
• Isenberg JS, Jia Y, Fukuyama J, et al. (2007b). Thrombospondin-1 inhibits nitric oxide signaling via CD36 by inhibiting myristic acid uptake. J Biol Chem 282:15404–15
   PubMed Web of Science ®Google Scholar
• Isenberg JS, Martin-Manso G, Maxhimer JB, Roberts DD. (2009b). Regulation of nitric oxide signalling by thrombospondin 1: implications for anti-angiogenic therapies. Nat Rev Cancer 9:182–94
   Google Scholar
• Isenberg JS, Maxhimer JB, Hyodo F, et al. (2008a). Thrombospondin-1 and CD47 limit cell and tissue survival of radiation injury. Am J Pathol 173:1100–12
   PubMed Web of Science ®Google Scholar
• Isenberg JS, Maxhimer JB, Powers P, et al. (2008b). Treatment of ischemia/reperfusion injury by limiting thrombospondin-1/CD47 signaling. Surgery 144:752–61
   PubMed Web of Science ®Google Scholar
• Isenberg JS, Pappan LK, Romeo MJ, et al. (2008c). Blockade of thrombospondin-1-CD47 interactions prevents necrosis of full thickness skin grafts. Ann Surg 247:180–90
   PubMed Web of Science ®Google Scholar
• Isenberg JS, Qin Y, Maxhimer JB, et al. (2009c). Thrombospondin-1 and CD47 regulate blood pressure and cardiac responses to vasoactive stress. Matrix Biol 28:110–19
   PubMed Web of Science ®Google Scholar
• Isenberg JS, Ridnour LA, Dimitry J, et al. (2006). CD47 is necessary for inhibition of nitric oxide-stimulated vascular cell responses by thrombospondin-1. J Biol Chem 281:26069–80
   PubMed Web of Science ®Google Scholar
• Isenberg JS, Romeo MJ, Abu-Asab M, et al. (2007c). Increasing survival of ischemic tissue by targeting CD47. Circ Res 100:712–20
   PubMed Web of Science ®Google Scholar
• Isenberg JS, Romeo MJ, Yu C, et al. (2008d). Thrombospondin-1 stimulates platelet aggregation by blocking the antithrombotic activity of nitric oxide/cGMP signaling. Blood 111:613–23
   PubMed Web of Science ®Google Scholar
• Ishihara M, Urushido M, Hamada K, et al. (2013). Sestrin-2 and BNIP3 regulate autophagy and mitophagy in renal tubular cells in acute kidney injury. Am J Physiol Renal Physiol 305:F495–509
   PubMed Web of Science ®Google Scholar
• Jin G, Tsuji K, Xing C, et al. (2009). CD47 gene knockout protects against transient focal cerebral ischemia in mice. Exp Neurol 217:165–70
   Google Scholar
• Kalas W, Swiderek E, Rapak A, et al. (2011). H-ras up-regulates expression of BNIP3. Anticancer Res 31:2869–75
   PubMed Web of Science ®Google Scholar
• Kalas W, Swiderek E, Switalska M, et al. (2013). Thrombospondin-1 receptor mediates autophagy of RAS-expressing cancer cells and triggers tumour growth inhibition. Anticancer Res 33:1429–38
   PubMed Web of Science ®Google Scholar
• Kaur S, Chang T, Singh SP, et al. (2014a). CD47 signaling regulates the immunosuppressive activity of VEGF in T cells. J Immunol 193:3914–24
   PubMed Web of Science ®Google Scholar
• Kaur S, Kuznetsova SA, Pendrak ML, et al. (2011). Heparan sulfate modification of the transmembrane receptor CD47 is necessary for inhibition of T cell receptor signaling by thrombospondin-1. J Biol Chem 286:14991–5002
   PubMed Web of Science ®Google Scholar
• Kaur S, Martin-Manso G, Pendrak ML, et al. (2010). Thrombospondin-1 inhibits vascular endothelial growth factor receptor-2 signaling by disrupting its association with CD47. J Biol Chem 285:38923–32
   PubMed Web of Science ®Google Scholar
• Kaur S, Singh SP, Elkahloun AG, et al. (2014b). CD47-dependent immunomodulatory and angiogenic activities of extracellular vesicles produced by T cells. Matrix Biol 37:49–59
   PubMed Web of Science ®Google Scholar
• Kaur S, Soto-Pantoja DR, Stein EV, et al. (2013). Thrombospondin-1 signaling through CD47 inhibits self-renewal by regulating c-Myc and other stem cell transcription factors. Sci Rep 3:1673. doi: 10.1038/srep01673
   PubMed Web of Science ®Google Scholar
• Kershaw MH, Smyth MJ. (2013). Immunology. Making macrophages eat cancer. Science 341:41–2
   Google Scholar
• Kim HS, Choi DY, Yun SJ, et al. (2012). Proteomic analysis of microvesicles derived from human mesenchymal stem cells. J Proteome Res 11:839–49
   PubMed Web of Science ®Google Scholar
• Kim MJ, Lee JC, Lee JJ, et al. (2008). Association of CD47 with natural killer cell-mediated cytotoxicity of head-and-neck squamous cell carcinoma lines. Tumour Biol 29:28–34
   PubMed Web of Science ®Google Scholar
• Kolluru GK, Shen X, Bir SC, Kevil CG. (2013). Hydrogen sulfide chemical biology: pathophysiological roles and detection. Nitric Oxide 35:5–20
   PubMed Web of Science ®Google Scholar
• Kosfeld MD, Frazier WA. (1993). Identification of a new cell adhesion motif in two homologous peptides from the COOH-terminal cell binding domain of human thrombospondin. J Biol Chem 268:8808–14
   PubMed Web of Science ®Google Scholar
• Kvansakul M, Adams JC, Hohenester E. (2004). Structure of a thrombospondin C-terminal fragment reveals a novel calcium core in the type 3 repeats. EMBO J 23:1223–33
   PubMed Web of Science ®Google Scholar
• Lamy L, Foussat A, Brown EJ, et al. (2007). Interactions between CD47 and thrombospondin reduce inflammation. J Immunol 178:5930–9
   PubMed Web of Science ®Google Scholar
• Lamy L, Ticchioni M, Rouquette-Jazdanian AK, et al. (2003). CD47 and the 19 kDa interacting protein-3 (BNIP3) in T cell apoptosis. J Biol Chem 278:23915–21
   PubMed Web of Science ®Google Scholar
• Latour S, Tanaka H, Demeure C, et al. (2001). Bidirectional negative regulation of human T and dendritic cells by CD47 and its cognate receptor signal-regulator protein-alpha: down-regulation of IL-12 responsiveness and inhibition of dendritic cell activation. J Immunol 167:2547–54
   PubMed Web of Science ®Google Scholar
• Leclair P, Lim CJ. (2014). CD47-independent effects mediated by the TSP-derived 4N1K peptide. PLoS One 9:e98358
   PubMedGoogle Scholar
• Lee DY, Arnott D, Brown EJ. (2013a). Ubiquilin4 is an adaptor protein that recruits Ubiquilin1 to the autophagy machinery. EMBO Rep 14:373–81
   PubMed Web of Science ®Google Scholar
• Lee JE, Jeon IS, Han NE, et al. (2013b). Ubiquilin 1 interacts with Orai1 to regulate calcium mobilization. Mol Cells 35:41–6
   PubMed Web of Science ®Google Scholar
• Li SS, Liu Z, Uzunel M, Sundqvist KG. (2006). Endogenous thrombospondin-1 is a cell surface ligand for regulation of integrin dependent T lymphocyte adhesion. Blood 108:3112–20
   PubMed Web of Science ®Google Scholar
• Li Z, Calzada MJ, Sipes JM, et al. (2002). Interactions of thrombospondins with a4b1 integrin and CD47 differentially modulate T cell behavior. J Cell Biol 157:509–19
   PubMed Web of Science ®Google Scholar
• Li Z, He L, Wilson KE, Roberts DD. (2001). Thrombospondin-1 inhibits TCR-mediated T lymphocyte early activation. J Immunol 166:2427–36
   PubMed Web of Science ®Google Scholar
• Lin Y, Manning PT, Jia J, et al. (2014). CD47 blockade reduces ischemia-reperfusion injury and improves outcomes in a rat kidney transplant model. Transplantation 98:394–401
   PubMed Web of Science ®Google Scholar
• Lindberg FP, Bullard DC, Caver TE, et al. (1996a). Decreased resistance to bacterial infection and granulocyte defects in IAP-deficient mice. Science 274:795–8
   PubMed Web of Science ®Google Scholar
• Lindberg FP, Gresham HD, Reinhold MI, Brown EJ. (1996b). Integrin-associated protein immunoglobulin domain is necessary for efficient vitronectin bead binding. J Cell Biol 134:1313–22
   PubMed Web of Science ®Google Scholar
• Lindberg FP, Gresham HD, Schwarz E, Brown EJ. (1993). Molecular cloning of integrin-associated protein: an immunoglobulin family member with multiple membrane-spanning domains implicated in alpha v beta 3-dependent ligand binding. J Cell Biol 123:485–96
   PubMed Web of Science ®Google Scholar
• Liu Y, Lu L, Hettinger CL, et al. (2014). Ubiquilin-1 protects cells from oxidative stress and ischemic stroke caused tissue injury in mice. J Neurosci 34:2813–21
   PubMed Web of Science ®Google Scholar
• Maile LA, Allen LB, Hanzaker CF, et al. (2010). Glucose regulation of thrombospondin and its role in the modulation of smooth muscle cell proliferation. Exp Diabetes Res 2010:pii:617052
   Google Scholar
• Maile LA, Capps BE, Miller EC, et al. (2008a). Integrin-associated protein association with SRC homology 2 domain containing tyrosine phosphatase substrate 1 regulates igf-I signaling in vivo. Diabetes 57:2637–43
   PubMed Web of Science ®Google Scholar
• Maile LA, Capps BE, Miller EC, et al. (2008b). Glucose regulation of integrin-associated protein cleavage controls the response of vascular smooth muscle cells to insulin-like growth factor-I. Mol Endocrinol 22:1226–37
   PubMed Web of Science ®Google Scholar
• Maile LA, Clemmons DR. (2003). Integrin-associated protein binding domain of thrombospondin-1 enhances insulin-like growth factor-I receptor signaling in vascular smooth muscle cells. Circ Res 93:925–31
   PubMed Web of Science ®Google Scholar
• Majeti R, Chao MP, Alizadeh AA, et al. (2009). CD47 is an adverse prognostic factor and therapeutic antibody target on human acute myeloid leukemia stem cells. Cell 138:286–99
   PubMed Web of Science ®Google Scholar
• Manna PP, Dimitry J, Oldenborg PA, Frazier WA. (2005). CD47 augments Fas/CD95-mediated apoptosis. J Biol Chem 280:29637–44
   PubMed Web of Science ®Google Scholar
• Manna PP, Frazier WA. (2003). The mechanism of CD47-dependent killing of T cells: heterotrimeric Gi-dependent inhibition of protein kinase A. J Immunol 170:3544–53
   PubMed Web of Science ®Google Scholar
• Martin-Manso G, Galli S, Ridnour LA, et al. (2008). Thrombospondin-1 promotes tumor macrophage recruitment and enhances tumor cell cytotoxicity by differentiated U937 cells. Cancer Res 68:7090–9
   PubMed Web of Science ®Google Scholar
• Martinelli R, Newton G, Carman CV, et al. (2013). Novel role of CD47 in rat microvascular endothelium: signaling and regulation of T-cell transendothelial migration. Arterioscler Thromb Vasc Biol 33:2566–76
   PubMed Web of Science ®Google Scholar
• Mateo V, Brown EJ, Biron G, et al. (2002). Mechanisms of CD47-induced caspase-independent cell death in normal and leukemic cells: link between phosphatidylserine exposure and cytoskeleton organization. Blood 100:2882–90
   PubMed Web of Science ®Google Scholar
• Matozaki T, Murata Y, Okazawa H, Ohnishi H. (2009). Functions and molecular mechanisms of the CD47-SIRPalpha signalling pathway. Trends Cell Biol 19:72–80
   PubMed Web of Science ®Google Scholar
• Mawby WJ, Holmes CH, Anstee DJ, et al. (1994). Isolation and characterization of CD47 glycoprotein: a multispanning membrane protein which is the same as integrin-associated protein (IAP) and the ovarian tumour marker OA3. Biochem J 304:525–30
   PubMed Web of Science ®Google Scholar
• Maxhimer JB, Shih HB, Isenberg JS, et al. (2009a). Thrombospondin-1-CD47 blockade following ischemia reperfusion injury is tissue protective. Plast Reconstr Surg 124:1880–9
   PubMed Web of Science ®Google Scholar
• Maxhimer JB, Soto-Pantoja DR, Ridnour LA, et al. (2009b). Radioprotection in normal tissue and delayed tumor growth by blockade of CD47 signaling. Sci Transl Med 1:3ra7
   PubMed Web of Science ®Google Scholar
• Mcdonald JF, Dimitry JM, Frazier WA. (2003). An amyloid-like C-terminal domain of thrombospondin-1 displays CD47 agonist activity requiring both VVM motifs. Biochemistry 42:10001–11
   PubMed Web of Science ®Google Scholar
• Mcdonald JF, Zheleznyak A, Frazier WA. (2004). Cholesterol-independent interactions with CD47 enhance alphavbeta3 avidity. J Biol Chem 279:17301–11
   PubMed Web of Science ®Google Scholar
• Miller TW, Isenberg JS, Roberts DD. (2010a). Thrombospondin-1 is an inhibitor of pharmacological activation of soluble guanylate cyclase. Br J Pharmacol 159:1542–7
   PubMed Web of Science ®Google Scholar
• Miller TW, Isenberg JS, Shih HB, et al. (2010b). Amyloid-beta inhibits No-cGMP signaling in a CD36- and CD47-dependent manner. PLoS One 5:e15686
   PubMed Web of Science ®Google Scholar
• Miller TW, Kaur S, Ivins-O'keefe K, Roberts DD. (2013). Thrombospondin-1 is a CD47-dependent endogenous inhibitor of hydrogen sulfide signaling in T cell activation. Matrix Biol 32:316–24
   PubMed Web of Science ®Google Scholar
• Miller TW, Wang EA, Gould S, et al. (2012). Hydrogen sulfide is an endogenous potentiator of T cell activation. J Biol Chem 287:4211–21
   Google Scholar
• Mittal R, Gonzalez-Gomez I, Prasadarao NV. (2010). Escherichia coli K1 promotes the ligation of CD47 with thrombospondin-1 to prevent the maturation of dendritic cells in the pathogenesis of neonatal meningitis. J Immunol 185:2998–3006
   PubMed Web of Science ®Google Scholar
• Miyashita M, Ohnishi H, Okazawa H, et al. (2004). Promotion of neurite and filopodium formation by CD47: roles of integrins, Rac, and Cdc42. Mol Biol Cell 15:3950–63
   PubMed Web of Science ®Google Scholar
• Mouro-Chanteloup I, Delaunay J, Gane P, et al. (2003). Evidence that the red cell skeleton protein 4.2 interacts with the Rh membrane complex member CD47. Blood 101:338–44
   PubMed Web of Science ®Google Scholar
• Mushegian A. (2002). Refining structural and functional predictions for secretasome components by comparative sequence analysis. Proteins 47:69–74
   PubMed Web of Science ®Google Scholar
• N'diaye EN, Brown EJ. (2003). The ubiquitin-related protein PLIC-1 regulates heterotrimeric G protein function through association with Gbetagamma. J Cell Biol 163:1157–65
   PubMed Web of Science ®Google Scholar
• Nishiyama Y, Tanaka T, Naitoh H, et al. (1997). Overexpression of integrin-associated protein (CD47) in rat kidney treated with a renal carcinogen, ferric nitrilotriacetate. Jpn J Cancer Res 88:120–8
   PubMedGoogle Scholar
• Nisoli E, Carruba MO. (2006). Nitric oxide and mitochondrial biogenesis. J Cell Sci 119:2855–62
   PubMed Web of Science ®Google Scholar
• Oldenborg PA, Gresham HD, Lindberg FP. (2001). CD47-signal regulatory protein alpha (SIRPalpha) regulates Fcgamma and complement receptor-mediated phagocytosis. J Exp Med 193:855–62
   PubMed Web of Science ®Google Scholar
• Oldenborg PA, Zheleznyak A, Fang YF, et al. (2000). Role of CD47 as a marker of self on red blood cells. Science 288:2051–4
   PubMed Web of Science ®Google Scholar
• Per-Arne O. (2012). Role of CD47 and signal regulatory protein alpha (SIRPalpha) in regulating the clearance of viable or aged blood cells. Transfus Med Hemother 39:315–20
   PubMed Web of Science ®Google Scholar
• Pettersen RD, Hestdal K, Olafsen MK, et al. (1999). CD47 signals T cell death. J Immunol 162:7031–40
   PubMed Web of Science ®Google Scholar
• Pfeiffer A, Bottcher A, Orso E, et al. (2001). Lipopolysaccharide and ceramide docking to CD14 provokes ligand-specific receptor clustering in rafts. Eur J Immunol 31:3153–64
   PubMed Web of Science ®Google Scholar
• Qin Q, Qian J, Ge L, et al. (2014). Effect and mechanism of thrombospondin-1 on the angiogenesis potential in human endothelial progenitor cells: an in vitro study. PLoS One 9:e88213
   PubMedGoogle Scholar
• Ramanathan S, Mazzalupo S, Boitano S, Montfort WR. (2011). Thrombospondin-1 and angiotensin II inhibit soluble guanylyl cyclase through an increase in intracellular calcium concentration. Biochemistry 50:7787–99
   PubMed Web of Science ®Google Scholar
• Rebres RA, Green JM, Reinhold MI, et al. (2001a). Membrane raft association of CD47 is necessary for actin polymerization and protein kinase C theta translocation in its synergistic activation of T cells. J Biol Chem 276:7672–80
   PubMed Web of Science ®Google Scholar
• Rebres RA, Kajihara K, Brown EJ. (2005). Novel CD47-dependent intercellular adhesion modulates cell migration. J Cell Physiol 205:182–93
   PubMed Web of Science ®Google Scholar
• Rebres RA, Vaz LE, Green JM, Brown EJ. (2001b). Normal ligand binding and signaling by CD47 (integrin-associated protein) requires a long range disulfide bond between the extracellular and membrane spanning domains. J Biol Chem 276:34607–16
   PubMed Web of Science ®Google Scholar
• Rho J, Chung J, Im H, et al. (2013). Magnetic nanosensor for detection and profiling of erythrocyte-derived microvesicles. ACS Nano 7:11227–33
   PubMed Web of Science ®Google Scholar
• Rogers NM, Thomson AW, Isenberg JS. (2012). Activation of parenchymal CD47 promotes renal ischemia-reperfusion injury. J Am Soc Nephrol 23:1538–50
   PubMed Web of Science ®Google Scholar
• Rothenberg C, Srinivasan D, Mah L, et al. (2010). Ubiquilin functions in autophagy and is degraded by chaperone-mediated autophagy. Hum Mol Genet 19:3219–32
   PubMed Web of Science ®Google Scholar
• Sadallah S, Eken C, Martin PJ, Schifferli JA. (2011). Microparticles (ectosomes) shed by stored human platelets downregulate macrophages and modify the development of dendritic cells. J Immunol 186:6543–52
   PubMed Web of Science ®Google Scholar
• Sarfati M, Fortin G, Raymond M, Susin S. (2008). CD47 in the immune response: role of thrombospondin and SIRP-alpha reverse signaling. Curr Drug Targets 9:842–50
   PubMed Web of Science ®Google Scholar
• Schon P, Vischer P, Volker W, et al. (1992). Cell-associated proteoheparan sulfate mediates binding and uptake of thrombospondin in cultured porcine vascular endothelial cells. Eur J Cell Biol 59:329–39
   PubMed Web of Science ®Google Scholar
• Schwartz MA, Brown EJ, Fazeli B. (1993). A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells. J Biol Chem 268:19931–4
   PubMed Web of Science ®Google Scholar
• Shaked Y, Bertolini F, Man S, et al. (2005). Genetic heterogeneity of the vasculogenic phenotype parallels angiogenesis; Implications for cellular surrogate marker analysis of antiangiogenesis. Cancer Cell 7:101–11
   PubMed Web of Science ®Google Scholar
• Sharifi-Sanjani M, Shoushtari AH, Quiroz M, et al. (2014). Cardiac CD47 drives left ventricular heart failure through Ca2+-CaMKII-regulated induction of HDAC3. J Am Heart Assoc 3:e000670
   Google Scholar
• Shibuya M. (2006). Differential roles of vascular endothelial growth factor receptor-1 and receptor-2 in angiogenesis. J Biochem Mol Biol 39:469–78
   PubMedGoogle Scholar
• Shinohara M, Ohyama N, Murata Y, et al. (2006). CD47 regulation of epithelial cell spreading and migration, and its signal transduction. Cancer Sci 97:889–95
   PubMed Web of Science ®Google Scholar
• Sick E, Boukhari A, Deramaudt T, et al. (2011). Activation of CD47 receptors causes proliferation of human astrocytoma but not normal astrocytes via an Akt-dependent pathway. Glia 59:308–19
   PubMed Web of Science ®Google Scholar
• Sick E, Jeanne A, Schneider C, et al. (2012). CD47 update: a multi-faceted actor in the tumour microenvironment of potential therapeutic interest. Br J Pharmacol 167:1415–30
   PubMed Web of Science ®Google Scholar
• Sipes JM, Krutzsch HC, Lawler J, Roberts DD. (1999). Cooperation between thrombospondin-1 type 1 repeat peptides and integrin avb3 ligands to promote melanoma cell spreading and focal adhesion formation. J Biol Chem 274:22755–62
   PubMed Web of Science ®Google Scholar
• Smadja DM, D'audigier C, Bieche I, et al. (2011). Thrombospondin-1 is a plasmatic marker of peripheral arterial disease that modulates endothelial progenitor cell angiogenic properties. Arterioscler Thromb Vasc Biol 31:551–9
   PubMed Web of Science ®Google Scholar
• Soto-Pantoja DR, Kaur S, Miller TW, et al. (2013a). Leukocyte surface antigen CD47. UCSD Molecule Pages 2:19–36
   Google Scholar
• Soto-Pantoja DR, Miller TW, Pendrak ML, et al. (2012). CD47 deficiency confers cell and tissue radioprotection by activation of autophagy. Autophagy 8:1628–42
   PubMed Web of Science ®Google Scholar
• Soto-Pantoja DR, Ridnour LA, Wink DA, Roberts DD. (2013b). Blockade of CD47 increases survival of mice exposed to lethal total body irradiation. Sci Rep 3:1038. doi: 10.1038/srep01038
   PubMed Web of Science ®Google Scholar
• Soto-Pantoja DR, Shih HB, Maxhimer JB, et al. (2014a). Thrombospondin-1 and CD47 signaling regulate healing of thermal injury in mice. Matrix Biol 37:25–34
   PubMed Web of Science ®Google Scholar
• Soto-Pantoja DR, Terabe M, Ghosh A, et al. (2014b). CD47 in the tumor microenvironment limits cooperation between antitumor T-cell immunity and radiotherapy. Cancer Res 74:6771–83
   PubMed Web of Science ®Google Scholar
• Su X, Johansen M, Looney MR, et al. (2008). CD47 deficiency protects mice from lipopolysaccharide-induced acute lung injury and Escherichia coli pneumonia. J Immunol 180:6947–53
   PubMed Web of Science ®Google Scholar
• Subramanian S, Boder ET, Discher DE. (2007). Phylogenetic divergence of CD47 interactions with human signal regulatory protein alpha reveals locus of species specificity. Implications for the binding site. J Biol Chem 282:1805–18
   PubMed Web of Science ®Google Scholar
• Subramanian S, Parthasarathy R, Sen S, et al. (2006a). Species- and cell type-specific interactions between CD47 and human SIRPalpha. Blood 107:2548–56
   PubMed Web of Science ®Google Scholar
• Subramanian S, Tsai R, Sen S, et al. (2006b). Membrane mobility and clustering of Integrin Associated Protein (IAP, CD47)--major differences between mouse and man and implications for signaling. Blood Cells Mol Dis 36:364–72
   PubMed Web of Science ®Google Scholar
• Swendeman S, Mendelson K, Weskamp G, et al. (2008). VEGF-A stimulates ADAM17-dependent shedding of VEGFR2 and crosstalk between VEGFR2 and ERK signaling. Circ Res 103:916–18
   PubMed Web of Science ®Google Scholar
• Takahashi K, Yamanaka S. (2006). Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors. Cell 126:663–76
   PubMed Web of Science ®Google Scholar
• Tibben JG, Massuger LF, Claessens RA, et al. (1992). Tumour detection and localization using 99Tcm-labelled OV-TL 3 Fab' in patients suspected of ovarian cancer. Nucl Med Commun 13:885–93
   PubMed Web of Science ®Google Scholar
• Tsai RK, Discher DE. (2008). Inhibition of “self” engulfment through deactivation of myosin-II at the phagocytic synapse between human cells. J Cell Biol 180:989–1003
   PubMed Web of Science ®Google Scholar
• Tulasne D, Judd BA, Johansen M, et al. (2001). C-terminal peptide of thrombospondin-1 induces platelet aggregation through the Fc receptor gamma-chain-associated signaling pathway and by agglutination. Blood 98:3346–52
   PubMed Web of Science ®Google Scholar
• Umemori H, Sanes JR. (2008). Signal regulatory proteins (SIRPS) are secreted presynaptic organizing molecules. J Biol Chem 283:34053–61
   PubMed Web of Science ®Google Scholar
• Unanue ER. (2013). Perspectives on anti-CD47 antibody treatment for experimental cancer. Proc Natl Acad Sci USA 110:10886–7
   PubMed Web of Science ®Google Scholar
• Van Kim CL, Colin Y, Cartron JP. (2006). Rh proteins: key structural and functional components of the red cell membrane. Blood Rev 20:93–110
   PubMed Web of Science ®Google Scholar
• Van Ravenswaay Claasen HH, Eggermont AM, Nooyen YA, et al. (1994). Immunotherapy in a human ovarian cancer xenograft model with two bispecific monoclonal antibodies: OV-TL 3/CD3 and OC/TR. Gynecol Oncol 52:199–206
   PubMed Web of Science ®Google Scholar
• Vasagiri N, Kutala VK. (2014). Structure, function, and epigenetic regulation of BNIP3: a pathophysiological relevance. Mol Biol Rep 41:7705–14
   PubMed Web of Science ®Google Scholar
• Verdrengh M, Lindberg FP, Ryden C, Tarkowski A. (1999). Integrin-associated protein (IAP)-deficient mice are less susceptible to developing Staphylococcus aureus-induced arthritis. Microbes Infect 1:745–51
   PubMed Web of Science ®Google Scholar
• Wang XQ, Lindberg FP, Frazier WA. (1999). Integrin-associated protein stimulates alpha2beta1-dependent chemotaxis via Gi-mediated inhibition of adenylate cyclase and extracellular-regulated kinases. J Cell Biol 147:389–400
   PubMed Web of Science ®Google Scholar
• Willingham SB, Volkmer JP, Gentles AJ, et al. (2012). The CD47-signal regulatory protein alpha (SIRPa) interaction is a therapeutic target for human solid tumors. Proc Natl Acad Sci USA 109:6662–7
   PubMed Web of Science ®Google Scholar
• Wu AL, Wang J, Zheleznyak A, Brown EJ. (1999). Ubiquitin-related proteins regulate interaction of vimentin intermediate filaments with the plasma membrane. Mol Cell 4:619–25
   PubMed Web of Science ®Google Scholar
• Xing C, Lee S, Kim WJ, et al. (2009). Role of oxidative stress and caspase 3 in CD47-mediated neuronal cell death. J Neurochem 108:430–6
   PubMed Web of Science ®Google Scholar
• Xu D, Fuster MM, Lawrence R, Esko JD. (2011). Heparan sulfate regulates VEGF165- and VEGF121-mediated vascular hyperpermeability. J Biol Chem 286:737–45
   PubMed Web of Science ®Google Scholar
• Yamauchi Y, Kuroki M, Imakiire T, et al. (2002). Opposite effects of thrombospondin-1 via CD36 and CD47 on homotypic aggregation of monocytic cells. Matrix Biol 21:441–8
   PubMed Web of Science ®Google Scholar
• Yao M, Roberts DD, Isenberg JS. (2011). Thrombospondin-1 inhibition of vascular smooth muscle cell responses occurs via modulation of both cAMP and cGMP. Pharmacol Res 63:13–22
   PubMed Web of Science ®Google Scholar
• Zhang X, Kazerounian S, Duquette M, et al. (2009). Thrombospondin-1 modulates vascular endothelial growth factor activity at the receptor level. FASEB J 23:3368–76
   PubMed Web of Science ®Google Scholar
• Zhang X, Lanahan AA, Simons M. (2013). VEGFR2 trafficking: speed doesn't kill. Cell Cycle 12:2163–4
   PubMed Web of Science ®Google Scholar